ID Q9XAV3_PSEFL Unreviewed; 1213 AA.
AC Q9XAV3;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 13-SEP-2023, entry version 101.
DE SubName: Full=Urea amidolyase homologue {ECO:0000313|EMBL:CAB48407.1};
GN Name=uahA {ECO:0000313|EMBL:CAB48407.1};
OS Pseudomonas fluorescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294 {ECO:0000313|EMBL:CAB48407.1};
RN [1] {ECO:0000313|EMBL:CAB48407.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DF57 {ECO:0000313|EMBL:CAB48407.1};
RA Jensen L.E., Koch B., Nybroe O.;
RT "A Pseudomonas homologue to the yeast urea amidolyase gene is regulated by
RT nitrogen but is not involved in urea metabolism.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AJ243652; CAB48407.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9XAV3; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000313|EMBL:CAB48407.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1133..1211
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1213 AA; 131583 MW; D08D36004126A01B CRC64;
MFEKILIANR GAIACRILRT LRELEVKGVA VYSQADAASL HIQQADEAYC LGDGAAAGTY
LAVDKLLAIA KSSGATAIHP GYGFLSENAA FAEACEAADI AFIGPTPEQL RVFGLKHTAR
DLARRHGVPL LEGTELLDSL DAALLAGTQL GYPVMLKSTA GGGGIGMRVC RSATDLSESF
EAVKRLGQNN FSDAGVFIEK YIERARHLEV QVFGDGQGQV IALGVRDCSV QRRNQKVLEE
TPAPNLPEGM ADELCAAAIQ LAQAVNYRSA GTVEFVFDSD AGRFYFLEVN TRLQVEHGVT
EQVWGVDLVR WMVQLAAGDL PPLSELGQGL KAEGHAIQAR LYAEDPGRDF QPSPGLLTAV
KFPQADGKAL RIDTWVEAGC QIPPYFDPMI AKVIRWAPTR EQARLGLHQA LDESLLYGVE
TNRHYLQQIL LDAPFASGQP WTRCLEALVY RANTVEVLSP GTQTSVQDYP GRLGYWAVGV
PPSGPMDSHS LRLGNRLLGN EEGAAALEIT MNGAAVRFNC DARVAVTGAV IALTLDGEAV
PMNTPLSIAA GSTLTIGTIA GAGARSYLCL QGGVQVPDYL GSKSTFTLGQ FGGHGGRALC
TGDVLHLTEL DEHAALPQQN APILELPSER QIRVIYGPHG APEYFTERYI QTFFDTAWEV
HFNSSRTGVR LIGPKPEWVR ADGGEAGLHP SNIHDNPYAI GAVDFTGDMP VILGPDGPSL
GGFVCPVTVI EADLWQLGQL KAGDKVRFVP VDISTARSLA LNWAPCGSEL ARDSGLSVSS
RLDVPPLSRA SSLPQGMGSP VVLDIGQDDT RLVARLAGDT HLLLEIGAAE LDLVLRFRAH
ALMQALEHKQ LPGVIDLTPG IRSLQVHYQP EQMPLADLLS IVVGEWDAVC AAQDLQVPSR
IVHLPLSWDD PACQLAIEKY MTTVRKDAPW CPSNLEFIRR INDLPNLDEV QRTVFDASYL
VMGLGDVYLG APVATPLDPR HRLVTTKYNP ARTWTAENSV GIGGAYMCVY GMEGPGGYQF
VGRTLQMWNR YREVAAFNGK PWLLRFFDQI RFYPVSADEL LHIRREFPLG RFDLKIEHSQ
LNLADYQRFL VQEADSIAAF RQQQQGAFNA ERERWIASGQ AHFDSEEPAV APSEDSLLTE
GQLSVDSHIA GNLWQVQVDV GARVAAGDVL VILESMKMEI PLLAPSAGVV REVRVQPGSA
VRAGQRVVVL DRA
//